Thermostable phenylalanine dehydrogenase from a mesophilic microbacterium sp. strain DM 86-1
Bacteria that produced NAD+-dependent phenylalanine dehydrogenase (EC 1.4.1.20) were selected among l-methionine utilizers isolated from soil. A bacterial strain showing phenylalanine dehydrogenase activity was chosen and classified in the genus Microbacterium. Phenylalanine dehydrogenase was purified from the crude extract of Microbacterium sp. strain DM 86-1 (TPU 3592) to homogeneity as judged by SDS-polyacrylamide disc gel electrophoresis. The enzyme has an isoelectric point of 5.8 and a relative molecular weight (Mr) of approximately 330,000. The enzyme is composed of eight identical subunits with an Mr of approximately 41,000. The apparent Km values for l-phenylalanine and NAD+ were calculated to be 0.10 mM and 0.20 mM, respectively. No loss of the enzyme activity was observed upon incubation at 55 degrees C for 10 min.
Asano
Y
Biotechnology Research Center, Toyama Prefectural University, 5180 Kurokawa, Kosugi, Toyama, 939-0398 Japan.
Tanetani
M